Palmitoylation of solute carriers.

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  • Author(s): Villanueva CE;Villanueva CE; Hagenbuch B; Hagenbuch B
  • Source:
    Biochemical pharmacology [Biochem Pharmacol] 2023 Sep; Vol. 215, pp. 115695. Date of Electronic Publication: 2023 Jul 20.
  • Publication Type:
    Journal Article; Review; Research Support, N.I.H., Extramural
  • Language:
    English
  • Additional Information
    • Source:
      Publisher: Elsevier Science Country of Publication: England NLM ID: 0101032 Publication Model: Print-Electronic Cited Medium: Internet ISSN: 1873-2968 (Electronic) Linking ISSN: 00062952 NLM ISO Abbreviation: Biochem Pharmacol Subsets: MEDLINE
    • Publication Information:
      Publication: Oxford : Elsevier Science
      Original Publication: Oxford, New York [etc.] Paragamon Press.
    • Subject Terms:
      Palmitic Acid*/metabolism ; Lipoylation*/physiology; Humans ; Protein Processing, Post-Translational ; Phosphorylation ; Membrane Proteins/metabolism ; Serotonin Plasma Membrane Transport Proteins/metabolism
    • Abstract:
      Post-translational modifications are an important mechanism in the regulation of protein expression, function, and degradation. Well-known post-translational modifications are phosphorylation, glycosylation, and ubiquitination. However, lipid modifications, including myristoylation, prenylation, and palmitoylation, are poorly studied. Since the early 2000s, researchers have become more interested in lipid modifications, especially palmitoylation. The number of articles in PubMed increased from about 350 between 2000 and 2005 to more than 600 annually during the past ten years. S-palmitoylation, where the 16-carbon saturated (C16:0) palmitic acid is added to free cysteine residues of proteins, is a reversible protein modification that can affect the expression, membrane localization, and function of the modified proteins. Various diseases like Huntington's and Alzheimer's disease have been linked to changes in protein palmitoylation. In humans, the addition of palmitic acid is mediated by 23 palmitoyl acyltransferases, also called DHHC proteins. The modification can be reversed by a few thioesterases or hydrolases. Numerous soluble and membrane-attached proteins are known to be palmitoylated, but among the approximately 400 solute carriers that are classified in 66 families, only 15 found in 8 families have so far been documented to be palmitoylated. Among the best-characterized transporters are the glucose transporters GLUT1 (SLC2A1) and GLUT4 (SLC2A4), the three monoamine transporters norepinephrine transporter (NET; SLC6A2), dopamine transporter (DAT; SLC6A3), and serotonin transporter (SERT; SLC6A4), and the sodium-calcium exchanger NCX1 (SLC8A1). While there is evidence from recent proteomics experiments that numerous solute carriers are palmitoylated, no details beyond the 15 transporters covered in this review are available.
      Competing Interests: Declaration of Competing Interest The authors declare that they have no known competing financial interests or personal relationships that could have appeared to influence the work reported in this paper.
      (Copyright © 2023 The Authors. Published by Elsevier Inc. All rights reserved.)
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    • Grant Information:
      R01 GM077336 United States GM NIGMS NIH HHS
    • Contributed Indexing:
      Keywords: Post-translational modification; S-palmitoylation; Solute carrier; Transport
    • Accession Number:
      2V16EO95H1 (Palmitic Acid)
      0 (Membrane Proteins)
      0 (SLC6A4 protein, human)
      0 (Serotonin Plasma Membrane Transport Proteins)
    • Publication Date:
      Date Created: 20230722 Date Completed: 20230906 Latest Revision: 20231003
    • Publication Date:
      20240829
    • Accession Number:
      PMC10530500
    • Accession Number:
      10.1016/j.bcp.2023.115695
    • Accession Number:
      37481134